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Protein

Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial

Gene

GPX6

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione.By similarity

Catalytic activityi

2 glutathione + a lipid hydroperoxide = glutathione disulfide + lipid + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei105 – 1051By similarity

GO - Molecular functioni

  1. glutathione peroxidase activity Source: TAIR
  2. phospholipid-hydroperoxide glutathione peroxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. response to cadmium ion Source: TAIR
  2. response to oxidative stress Source: InterPro
  3. response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Stress response

Enzyme and pathway databases

ReactomeiREACT_319433. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_336963. Synthesis of 5-eicosatetraenoic acids.

Protein family/group databases

PeroxiBasei2502. AtGPx06.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial (EC:1.11.1.12)
Short name:
AtGPX1
Short name:
PHGPx
Gene namesi
Name:GPX6
Synonyms:GPX1
Ordered Locus Names:At4g11600
ORF Names:T5C23.30
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G11600.

Subcellular locationi

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. chloroplast Source: TAIR
  3. cytosol Source: TAIR
  4. mitochondrion Source: TAIR
  5. plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5454MitochondrionSequence AnalysisAdd
BLAST
Chaini55 – 232178Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrialPRO_0000013088Add
BLAST

Proteomic databases

PaxDbiO48646.
PRIDEiO48646.

Expressioni

Tissue specificityi

Expressed at a low but detectable level in leaves, stems, and flowers, but at a higher level in siliques and even higher in roots. Predominantly expressed in seeds.2 Publications

Inductioni

By salt stress, osmotic stress, cold treatment, and metals. Up-regulated by salicylic acid (SA), jasmonic acid (JA), abscisic acid (ABA) and auxin.3 Publications

Gene expression databases

GenevestigatoriO48646.

Interactioni

Protein-protein interaction databases

BioGridi12064. 1 interaction.
IntActiO48646. 2 interactions.
STRINGi3702.AT4G11600.1-P.

Structurei

3D structure databases

ProteinModelPortaliO48646.
SMRiO48646. Positions 71-230.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0386.
HOGENOMiHOG000277054.
InParanoidiO48646.
KOiK00432.
OMAiPGNEGAI.
PhylomeDBiO48646.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O48646-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRSSIRLLY IRRTSPLLRS LSSSSSSSSS KRFDSAKPLF NSHRIISLPI
60 70 80 90 100
STTGAKLSRS EHSMAASSEP KSLYDFTVKD AKGNDVDLSI YKGKVLLIVN
110 120 130 140 150
VASQCGLTNS NYTELAQLYE KYKGHGFEIL AFPCNQFGNQ EPGTNEEIVQ
160 170 180 190 200
FACTRFKAEY PIFDKVDVNG DKAAPVYKFL KSSKGGLFGD GIKWNFAKFL
210 220 230
VDKDGNVVDR FAPTTSPLSI EKDVKKLLGV TA
Length:232
Mass (Da):25,584
Last modified:May 9, 2004 - v2
Checksum:i93F3084A8A331494
GO

Sequence cautioni

The sequence AAC09173.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAM66969.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA24226.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAB39931.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAB78203.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301S → SSSS (Ref. 1) Curated
Sequence conflicti51 – 511S → Y (PubMed:9511228).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030132 mRNA. Translation: AAC09173.1. Different initiation.
AL049500 Genomic DNA. Translation: CAB39931.1. Different initiation.
AL161532 Genomic DNA. Translation: CAB78203.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE83029.1.
AY039863 mRNA. Translation: AAK63967.1.
AY077655 mRNA. Translation: AAL76133.1.
AY088647 mRNA. Translation: AAM66969.1. Different initiation.
AB001568 mRNA. Translation: BAA24226.1. Different initiation.
PIRiT04207.
RefSeqiNP_192897.2. NM_117229.3.
UniGeneiAt.23184.

Genome annotation databases

EnsemblPlantsiAT4G11600.1; AT4G11600.1; AT4G11600.
GeneIDi826765.
KEGGiath:AT4G11600.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF030132 mRNA. Translation: AAC09173.1. Different initiation.
AL049500 Genomic DNA. Translation: CAB39931.1. Different initiation.
AL161532 Genomic DNA. Translation: CAB78203.1. Different initiation.
CP002687 Genomic DNA. Translation: AEE83029.1.
AY039863 mRNA. Translation: AAK63967.1.
AY077655 mRNA. Translation: AAL76133.1.
AY088647 mRNA. Translation: AAM66969.1. Different initiation.
AB001568 mRNA. Translation: BAA24226.1. Different initiation.
PIRiT04207.
RefSeqiNP_192897.2. NM_117229.3.
UniGeneiAt.23184.

3D structure databases

ProteinModelPortaliO48646.
SMRiO48646. Positions 71-230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi12064. 1 interaction.
IntActiO48646. 2 interactions.
STRINGi3702.AT4G11600.1-P.

Protein family/group databases

PeroxiBasei2502. AtGPx06.

Proteomic databases

PaxDbiO48646.
PRIDEiO48646.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G11600.1; AT4G11600.1; AT4G11600.
GeneIDi826765.
KEGGiath:AT4G11600.

Organism-specific databases

GeneFarmi2055. 163.
TAIRiAT4G11600.

Phylogenomic databases

eggNOGiCOG0386.
HOGENOMiHOG000277054.
InParanoidiO48646.
KOiK00432.
OMAiPGNEGAI.
PhylomeDBiO48646.

Enzyme and pathway databases

ReactomeiREACT_319433. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_336963. Synthesis of 5-eicosatetraenoic acids.

Gene expression databases

GenevestigatoriO48646.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a cDNA encoding a putative glutathione peroxidase protein from Arabidopsis thaliana."
    Bilodeau P., Luo M., Dennis E.S., Peacock W.J., Chaudhury A.M.
    Plant Gene Register PGR98-047
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Landsberg erecta.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-232.
  6. "Putative phospholipid hydroperoxide glutathione peroxidase gene from Arabidopsis thaliana induced by oxidative stress."
    Sugimoto M., Sakamoto W.
    Genes Genet. Syst. 72:311-316(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-232, INDUCTION.
    Strain: cv. Columbia.
  7. "Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated by abiotic stresses through diverse signaling pathways."
    Rodriguez Milla M.A., Maurer A., Rodriguez Huete A., Gustafson J.P.
    Plant J. 36:602-615(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY, INDUCTION.

Entry informationi

Entry nameiGPX6_ARATH
AccessioniPrimary (citable) accession number: O48646
Secondary accession number(s): Q94BV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 26, 2002
Last sequence update: May 9, 2004
Last modified: March 31, 2015
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.